2scu
From Proteopedia
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| == Structural highlights == | == Structural highlights == | ||
| <table><tr><td colspan='2'>[[2scu]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2SCU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2SCU FirstGlance]. <br> | <table><tr><td colspan='2'>[[2scu]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2SCU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2SCU FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | 
| - | <tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NEP:N1-PHOSPHONOHISTIDINE'>NEP</scene></td></tr> | + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NEP:N1-PHOSPHONOHISTIDINE'>NEP</scene></td></tr> | 
| - | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1scu|1scu]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1scu|1scu]]</td></tr> | 
| - | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Succinate--CoA_ligase_(ADP-forming) Succinate--CoA ligase (ADP-forming)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.2.1.5 6.2.1.5] </span></td></tr> | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Succinate--CoA_ligase_(ADP-forming) Succinate--CoA ligase (ADP-forming)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.2.1.5 6.2.1.5] </span></td></tr> | 
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2scu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2scu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2scu RCSB], [http://www.ebi.ac.uk/pdbsum/2scu PDBsum]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2scu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2scu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2scu RCSB], [http://www.ebi.ac.uk/pdbsum/2scu PDBsum]</span></td></tr> | 
| - | <table> | + | </table> | 
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/SUCD_ECOLI SUCD_ECOLI]] During aerobic metabolism it functions in the citric acid cycle, coupling the hydrolysis of succinyl-CoA to the synthesis of ATP and thus represents an important site of substrate-level phosphorylation. It can also function in the other direction for anabolic purposes, and this may be particularly important for providing succinyl-CoA during anaerobic growth when the oxidative route from 2-oxoglutarate is severely repressed. The alpha-subunit binds CoA, as well as ATP and catalyzes phosphoryl transfer to one of its histidine residues. The complete active site is probably located in the region of alpha-beta contact. [[http://www.uniprot.org/uniprot/SUCC_ECOLI SUCC_ECOLI]] During aerobic metabolism it functions in the citric acid cycle, coupling the hydrolysis of succinyl-CoA to the synthesis of ATP and thus represents an important site of substrate-level phosphorylation. It can also function in the other direction for anabolic purposes, and this may be particularly important for providing succinyl-CoA during anaerobic growth when the oxidative route from 2-oxoglutarate is severely repressed. The beta-subunit contains the attachment sites for succinate. The complete active site is probably located in the region of alpha-beta contact.  | ||
| == Evolutionary Conservation == | == Evolutionary Conservation == | ||
| [[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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| </StructureSection> | </StructureSection> | ||
| [[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
| - | [[Category: Bridger, W A | + | [[Category: Bridger, W A]] | 
| - | [[Category: Fraser, M E | + | [[Category: Fraser, M E]] | 
| - | [[Category: James, M N.G | + | [[Category: James, M N.G]] | 
| - | [[Category: Wolodko, W T | + | [[Category: Wolodko, W T]] | 
| [[Category: Citric acid cycle]] | [[Category: Citric acid cycle]] | ||
| [[Category: Heterotetramer]] | [[Category: Heterotetramer]] | ||
| [[Category: Ligase]] | [[Category: Ligase]] | ||
Revision as of 12:08, 25 December 2014
A detailed description of the structure of Succinyl-COA synthetase from Escherichia coli
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